FER Protein, Human (sf9, GST)

FER is a tyrosine-protein kinase that functions downstream of cell surface receptors for growth factors, playing roles in regulating the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration, and chemotaxis. It acts downstream of EGFR, KIT, PDGFRA, and PDGFRB, promoting NF-kappa-B activation and cell proliferation via EGFR. FER may regulate the mitotic cell cycle and is involved in the insulin receptor signaling pathway and phosphatidylinositol 3-kinase activation. Additionally, FER acts downstream of the activated FCER1 receptor, participating in FCER1-mediated signaling in mast cells and regulating mast cell degranulation. It also contributes to leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). In synapse organization, FER is involved in synaptic vesicle trafficking, excitatory postsynaptic current generation, and neuron-neuron synaptic transmission. It plays a role in neuronal cell death following brain damage. FER phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1, and PTPN11, may phosphorylate JUP and PTPN1, and can phosphorylate STAT3, though its biological relevance varies by cell type and stimulus.